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Literature summary for 3.5.1.88 extracted from

  • Dong, M.; Liu, H.
    Origins of the different metal preferences of Escherichia coli peptide deformylase and Bacillus thermoproteolyticus thermolysin: a comparative quantum mechanical/molecular mechanical study (2008), J. Phys. Chem. B, 112, 10280-10290.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
(S)-2-O-(phosphonoxy)-L-caproyl-L-leucyl-p-nitroanilide
-
Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+
-
Escherichia coli
Zn2+
-
Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli catalyzes the deformylation of nascent peptides in bacteria ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A6K3
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
formyl-Met-Gly-Gly-CH3 + H2O substrate used in QM-MM model Escherichia coli formate + Met-Gly-Gly-CH3
-
?
additional information catalyzes the deformylation of nascent peptides in bacteria Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
peptide deformylase
-
Escherichia coli